推荐产品
生物来源
Porcine brain
质量水平
检测方案
≥85%
形式
powder
溶解性
water: 50 mg/mL, clear, colorless to faintly yellow
储存温度
−20°C
SMILES字符串
CC(=O)c1ccc[n+](c1)[C@@H]2O[C@H](COP([O-])(=O)OP(O)(=O)OC[C@H]3O[C@H]([C@H](O)[C@@H]3O)n4cnc5c(N)ncnc45)[C@@H](O)[C@H]2O
InChI
1S/C22H28N6O14P2/c1-10(29)11-3-2-4-27(5-11)21-17(32)15(30)12(40-21)6-38-43(34,35)42-44(36,37)39-7-13-16(31)18(33)22(41-13)28-9-26-14-19(23)24-8-25-20(14)28/h2-5,8-9,12-13,15-18,21-22,30-33H,6-7H2,1H3,(H3-,23,24,25,34,35,36,37)/t12-,13-,15-,16-,17-,18-,21-,22-/m1/s1
InChI key
KPVQNXLUPNWQHM-RBEMOOQDSA-N
一般描述
3-乙酰吡啶腺嘌呤二核苷酸是一种结晶固体。3-乙酰吡啶腺嘌呤二核苷酸在各种交替氧化的酶活动中是一种突出的电子转运体。 APAD比NAD具有更显著的氧化电势。 NAD类似物APAD在电化学上比真正的NAD更有效地还原，其还原产物的稳定性也显著高于NADH。 在与NADH或NADPH的转氢化过程中，APAD也作为质子受体起作用。
应用
许多分子使用3-乙酰吡啶腺嘌呤二核苷酸作为信号分子、辅因子或底物。各种脱氢酶过程使用APAD代替NAD作为氢接受辅因子。 氧化磷酸化可以用ADAP进行研究。 ADAP也可以用作合适的底物。
生化/生理作用
APAD是一种NAD类似物，具有比NAD高的氧化电位。在许多脱氢酶反应中可代替 NAD 作为受氢辅助因子；例如， 弓形虫、华支睾吸虫、 和 疟原虫 中的乳酸脱氢酶、细菌硫辛酰胺脱氢酶以及哺乳动物脱氢酶。在与 NADH 或 NADPH 的各种转氢反应中也可作为质子受体。
联系
NAD 类似物
警示用语：
Warning
危险声明
危险分类
Eye Irrit. 2 - Skin Irrit. 2 - STOT SE 3
靶器官
Respiratory system
WGK
WGK 3
闪点(°F)
Not applicable
闪点(°C)
Not applicable
W A Prütz et al.
Archives of biochemistry and biophysics, 380(1), 181-191 (2000-07-20)
Degradation of the reduced pyridine nucleotides NMNH and NADH by HOCl involves two distinct stages: a fast reaction, k = 4.2 x 10(5) M(-1) s(-1), leads to generation of stable pyridine products (Py/Cl) with a strong absorption band at 275
Kinetic studies of Escherichia coli AlkB using a new fluorescence-based assay for DNA demethylation.
Todd W Roy et al.
Nucleic acids research, 35(21), e147-e147 (2007-11-16)
The Escherichia coli AlkB protein catalyzes the direct reversal of alkylation damage to DNA; primarily 1-methyladenine (1mA) and 3-methylcytosine (3mC) lesions created by endogenous or environmental alkylating agents. AlkB is a member of the non-heme iron (II) alpha-ketoglutarate-dependent dioxygenase superfamily
C O Hewitt et al.
Protein engineering, 10(1), 39-44 (1997-01-01)
This paper describes the testing of a homology model of Plasmodium falciparum lactate dehydrogenase (pfLDH) by protein engineering. The model had been validated in structural terms. It suggests explanations of the unusual properties of pfLDH (compared with all other LDHs).
M Yamaguchi et al.
Biochimica et biophysica acta, 1318(1-2), 225-234 (1997-01-16)
The hydrophilic, extramembranous domains I (alpha 1 subunit) and III of the Rhodospirillum rubrum nicotinamide nucleotide transhydrogenase were expressed in Escherichia coli and purified therefrom as soluble proteins. These domains bind NAD(H) and NADP(H). respectively, and together they form the
P D Bragg et al.
Archives of biochemistry and biophysics, 363(1), 182-190 (1999-03-02)
The pyridine nucleotide transhydrogenase carries out transmembrane proton translocation coupled to transfer of a hydride ion equivalent between NAD+ and NADP+. Previous workers (E. Holmberg et al. Biochemistry 33, 7691-7700, 1994; N. A. Glavas et al. Biochemistry 34, 7694-7702, 1995)
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